Evidence map›Paper›PMID 20937825›Full record

ArticleThe Journal of biological chemistry2010

Abl kinases are required for invadopodia formation and chemokine-induced invasion.

Pameeka S Smith-Pearson, Emileigh K Greuber, Gouri Yogalingam, Ann Marie Pendergast

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 78 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Pameeka S Smith-PearsonDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Emileigh K Greuber
Gouri Yogalingam
Ann Marie Pendergast
Duke University Hospital · USDuke Medical Center · US

Funding

MOLECULAR BASIS OF SIGNALING BY THE CABL PROTO-ONCOGENER01CA070940 · NCI · DUKE UNIVERSITY · PI PENDERGAST, ANN MARIE · 1996 to 2010
$3.4M
Intercellular adhesion and morphogenesis: role of actin-regulatory proteinsR01HL084102 · NHLBI · DUKE UNIVERSITY · PI PENDERGAST, ANN MARIE · 2007 to 2010
$1.5M
NCI NIH HHS CA 70940NCI NIH HHS R01 CA070940NHLBI NIH HHS HL 084102NHLBI NIH HHS R01 HL084102
6 · The paper itself

Abstract

The Abl tyrosine kinases, Abl and Arg, play a role in the regulation of the actin cytoskeleton by modulating cell-cell adhesion and cell motility. Deregulation of both the actin cytoskeleton and Abl kinases have been implicated in cancers. Abl kinase activity is elevated in a number of metastatic cancers and these kinases are activated downstream of several oncogenic growth factor receptor signaling pathways. However, the role of Abl kinases in regulation of the actin cytoskeleton during tumor progression and invasion remains elusive. Here we identify the Abl kinases as essential regulators of invadopodia assembly and function. We show that Abl kinases are activated downstream of the chemokine receptor, CXCR4, and are required for cancer cell invasion and matrix degradation induced by SDF1α, serum growth factors, and activated Src kinase. Moreover, Abl kinases are readily detected at invadopodia assembly sites and their inhibition prevents the assembly of actin and cortactin into organized invadopodia structures. We show that active Abl kinases form complexes with membrane type-1 matrix metalloproteinase (MT1-MMP), a critical invadopodia component required for matrix degradation. Further, loss of Abl kinase signaling induces internalization of MT1-MMP from the cell surface, promotes its accumulation in the perinuclear compartment and inhibits MT1-MMP tyrosine phosphorylation. Our findings reveal that Abl kinase signaling plays a critical role in invadopodia formation and function, and have far-reaching implications for the treatment of metastatic carcinomas.

Indexed as

AnimalsCell Line, TumorCell Surface ExtensionsChemokine CXCL12Extracellular MatrixHumansMatrix Metalloproteinase 14MiceNeoplasm InvasivenessNeoplasm MetastasisNeoplasmsNIH 3T3 CellsPhosphorylationProto-Oncogene Proteins c-ablReceptors, CXCR4Signal TransductionChemokine CXCL12CXCL12 protein, humanCxcl12 protein, mouseCXCR4 protein, humanCXCR4 protein, mouseMatrix Metalloproteinase 14MMP14 protein, humanMmp14 protein, mouseProto-Oncogene Proteins c-ablReceptors, CXCR4src-Family Kinases

Identifiers

PMID20937825
PMCPMC3001002
OpenAlexW1965457703

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.